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. 1996 Apr 2;93(7):3143–3148. doi: 10.1073/pnas.93.7.3143

Conformations and folding of lysozyme ions in vacuo.

D S Gross 1, P D Schnier 1, S E Rodriguez-Cruz 1, C K Fagerquist 1, E R Williams 1
PMCID: PMC39776  PMID: 8610183

Abstract

Proton transfer reactivity of isolated charge states of the protein hen egg-white lysozyme shows that multiple distinct conformations of this protein are stable in the gas phase. The reactivities of the 9+ and 10+ charge state ions, formed by electrospray ionization of "native" (disulfide-intact) and "denatured" (disulfide-reduced) solutions, are consistent with values calculated for ions in their crystal structure and fully denatured conformations, respectively. Charge states below 8+ of both forms, formed by proton stripping, have similar or indistinguishable reactivities, indicating that the disulfide-reduced ions fold in the gas phase to a more compact conformation.

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Selected References

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